Chasing the open-state structure of pentameric ligand-gated ion channels.

ABSTRACT: Remarkable advances have been made toward the structural characterization of ion channels in the last two decades. However, the unambiguous assignment of well-defined functional states to the obtained structural models has proved challenging. In the case of the superfamily of nicotinic-receptor channels (also referred to as pentameric ligand-gated ion channels [pLGICs]), for example, two different types of model of the open-channel conformation have been proposed on the basis of structures solved to resolutions better than 4.0 Å. At the level of the transmembrane pore, the open-state models of the proton-gated pLGIC from Gloeobacter violaceus (GLIC) and the invertebrate glutamate-gated Cl^- channel (GluCl) are very similar to each other, but that of the glycine receptor (G

SUBMITTER: Gonzalez-Gutierrez G 

PROVIDER: S-EPMC5715906 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature